Summary: TAP C-terminal domain
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|Nuclear RNA export factor 1|
|Symbols||; MEX67; TAP|
|RNA expression pattern|
This gene is one member of a family of nuclear RNA export factor genes. Common domain features of this family are a noncanonical RNP-type RNA-binding domain (RBD), 4 leucine-rich repeats (LRRs), a nuclear transport factor 2 (NTF2)-like domain that allows heterodimerization with NTF2-related export protein-1 (NXT1), and a ubiquitin-associated domain that mediates interactions with nucleoporins. Alternative splicing results in transcript variants. The LRRs and NTF2-like domains are required for export activity. The encoded protein of this gene shuttles between the nucleus and the cytoplasm and binds in vivo to poly(A)+ RNA. It is the vertebrate homologue of the yeast protein Mex67p. The encoded protein overcomes the mRNA export block caused by the presence of saturating amounts of CTE (constitutive transport element) RNA of type D retroviruses. A variant allele of the homologous Nxf1 gene in mice suppresses a class of mutations caused by integration of an endogenous retrovirus (intracisternal A particle) into an intron.
complex between tap uba domain and fxfg nucleoporin peptide
- vertebrate mRNA export factor TAP or nuclear RNA export factor 1 (NXF1).
- Caenorhabditis elegans nuclear RNA export factor 1 (nxf-1).
- yeast mRNA export factor MEX67. Members of the NXF family have a modular structure. A nuclear localization sequence and a noncanonical RNA recognition motif (RRM) (see PROSITEDOC) followed by four LRR repeats are located in its N-terminal half. The C-terminal half contains a NTF2 domain (see [href="http://expasy.org/prosite/PDOC50177 PROSITEDOC]) followed by a second domain, TAP-C. The TAP-C domain is important for binding to FG repeat-containing nuclear pore proteins (FG-nucleoporins) and is sufficient to mediate nuclear shuttling.
The Tap-C domain is made of four alpha helices packed against each other. The arrangement of helices 1, 2 and 3 is similar to that seen in a UBA fold. and is joined to the next module by flexible 12-residue Pro-rich linker.
Nuclear export of mRNAs is mediated by the Tap protein.
Tap can form a multimeric complex with itself and with other members of the NXF family. Three functional domains of Tap have been well characterized: the RNA-binding domain, the Nuclear Transport Factor 2 (NTF2)-like domain, and the ubiquitin-associated (UBA) domain.
- Yoon DW, Lee H, Seol W, DeMaria M, Rosenzweig M, Jung JU (May 1997). "Tap: a novel cellular protein that interacts with tip of herpesvirus saimiri and induces lymphocyte aggregation". Immunity 6 (5): 571–82. doi:10.1016/S1074-7613(00)80345-3. PMID 9175835.
- Grüter P, Tabernero C, von Kobbe C, et al. (April 1998). "TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export from the nucleus". Mol. Cell 1 (5): 649–59. doi:10.1016/S1097-2765(00)80065-9. PMID 9660949.
- Katahira J, Strässer K, Podtelejnikov A, Mann M, Jung JU, Hurt E (May 1999). "The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human". EMBO J. 18 (9): 2593–609. doi:10.1093/emboj/18.9.2593. PMC 1171339. PMID 10228171.
- "Entrez Gene: NXF1 nuclear RNA export factor 1".
- Floyd JA, Gold DA, Concepcion D, Poon TH, Wang X, Keithley E, Chen D, Ward EJ, Chinn SB, Friedman RA, Yu HT, Moriwaki K, Shiroishi T, Hamilton BA (November 2003). "A natural allele of Nxf1 suppresses retrovirus insertional mutations". Nat. Genet. 35 (3): 221–8. doi:10.1038/ng1247. PMC 2756099. PMID 14517553.
- Concepcion D, Flores-García L, Hamilton BA (May 2009). "Multipotent genetic suppression of retrotransposon-induced mutations by Nxf1 through fine-tuning of alternative splicing". In Frankel, Wayne N. PLoS Genet. 5 (5): e1000484. doi:10.1371/journal.pgen.1000484. PMC 2674570. PMID 19436707.
- Shamsher, Monee K; Ploski Jonathan; Radu Aurelian (October 2002). "Karyopherin beta 2B participates in mRNA export from the nucleus". Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (22): 14195–9. doi:10.1073/pnas.212518199. ISSN 0027-8424. PMC 137860. PMID 12384575.
- Kataoka, N; Diem M D; Kim V N; Yong J; Dreyfuss G (November 2001). "Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex". EMBO J. (England) 20 (22): 6424–33. doi:10.1093/emboj/20.22.6424. ISSN 0261-4189. PMC 125744. PMID 11707413.
- Zolotukhin, Andrei S; Tan Wei; Bear Jenifer; Smulevitch Sergey; Felber Barbara K (February 2002). "U2AF participates in the binding of TAP (NXF1) to mRNA". J. Biol. Chem. (United States) 277 (6): 3935–42. doi:10.1074/jbc.M107598200. ISSN 0021-9258. PMID 11724776.
- Tang, H; Wong-Staal F (October 2000). "Specific interaction between RNA helicase A and Tap, two cellular proteins that bind to the constitutive transport element of type D retrovirus". J. Biol. Chem. (UNITED STATES) 275 (42): 32694–700. doi:10.1074/jbc.M003933200. ISSN 0021-9258. PMID 10924507.
- Saito, Kuniaki; Fujiwara Toshinobu; Katahira Jun; Inoue Kunio; Sakamoto Hiroshi (August 2004). "TAP/NXF1, the primary mRNA export receptor, specifically interacts with a neuronal RNA-binding protein HuD". Biochem. Biophys. Res. Commun. (United States) 321 (2): 291–7. doi:10.1016/j.bbrc.2004.06.140. ISSN 0006-291X. PMID 15358174.
- Herold, A; Suyama M; Rodrigues J P; Braun I C; Kutay U; Carmo-Fonseca M; Bork P; Izaurralde E (December 2000). "TAP (NXF1) belongs to a multigene family of putative RNA export factors with a conserved modular architecture". Mol. Cell. Biol. (UNITED STATES) 20 (23): 8996–9008. doi:10.1128/MCB.20.23.8996-9008.2000. ISSN 0270-7306. PMC 86553. PMID 11073998.
- Schmitt, I; Gerace L (November 2001). "In vitro analysis of nuclear transport mediated by the C-terminal shuttle domain of Tap". J. Biol. Chem. (United States) 276 (45): 42355–63. doi:10.1074/jbc.M103916200. ISSN 0021-9258. PMID 11551912.
- Grant RP, Hurt E, Neuhaus D, Stewart M (April 2002). "Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1". Nat. Struct. Biol. 9 (4): 247–51. doi:10.1038/nsb773. PMID 11875519.
- Suyama M, Doerks T, Braun IC, Sattler M, Izaurralde E, Bork P (July 2000). "Prediction of structural domains of TAP reveals details of its interaction with p15 and nucleoporins". EMBO Rep. 1 (1): 53–8. doi:10.1038/sj.embor.embor627. PMC 1083685. PMID 11256625.
TAP C-terminal domain Provide feedback
The vertebrate Tap protein is a member of the NXF family of shuttling transport receptors for nuclear export of mRNA. Tap has a modular structure, and its most C-terminal domain is important for binding to FG repeat-containing nuclear pore proteins (FG-nucleoporins) and is sufficient to mediate nuclear shuttling . The structure of the C-terminal domain is composed of four helices . The structure is related to the UBA domain.
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR005637
The vertebrate Tap protein is a member of the NXF family of shuttling transport receptors for nuclear export of mRNA. Tap has a modular structure, and its most C-terminal domain is important for binding to FG repeat-containing nuclear pore proteins (FG-nucleoporins) and is sufficient to mediate nuclear shuttling [PUBMED:11875519]. The structure of the C-terminal domain is composed of four helices [PUBMED:11875519]. The structure is related to the UBA domain.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||nucleus (GO:0005634)|
|Biological process||mRNA transport (GO:0051028)|
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Curation and family details
|Seed source:||Bateman A|
|Number in seed:||8|
|Number in full:||365|
|Average length of the domain:||49.80 aa|
|Average identity of full alignment:||36 %|
|Average coverage of the sequence by the domain:||8.36 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||8|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the TAP_C domain has been found. There are 4 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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